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2og7
From Proteopedia
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| - | [[Image:2og7.gif|left|200px]] | + | [[Image:2og7.gif|left|200px]] |
| - | + | ||
| - | '''Cystal structure of asparagine oxygenase in complex with Fe(II), 2S,3S-3-hydroxyasparagine and succinate''' | + | {{Structure |
| + | |PDB= 2og7 |SIZE=350|CAPTION= <scene name='initialview01'>2og7</scene>, resolution 1.660Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> and <scene name='pdbligand=SIN:SUCCINIC ACID'>SIN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= sco3236 (asnO) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2 Bacteria]) | ||
| + | }} | ||
| + | |||
| + | '''Cystal structure of asparagine oxygenase in complex with Fe(II), 2S,3S-3-hydroxyasparagine and succinate''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2OG7 is a [ | + | 2OG7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OG7 OCA]. |
==Reference== | ==Reference== | ||
| - | Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide., Strieker M, Kopp F, Mahlert C, Essen LO, Marahiel MA, ACS Chem Biol. 2007 Mar 20;2(3):187-96. PMID:[http:// | + | Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide., Strieker M, Kopp F, Mahlert C, Essen LO, Marahiel MA, ACS Chem Biol. 2007 Mar 20;2(3):187-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17373765 17373765] |
[[Category: Bacteria]] | [[Category: Bacteria]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 19: | Line 28: | ||
[[Category: nonribosomal peptide synthesis; non-heme iron(ii); alpha-ketoglutarate oxygenase; beta-hydroxylated amino acid]] | [[Category: nonribosomal peptide synthesis; non-heme iron(ii); alpha-ketoglutarate oxygenase; beta-hydroxylated amino acid]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:59:17 2008'' |
Revision as of 15:59, 20 March 2008
| |||||||
| , resolution 1.660Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | sco3236 (asnO) (Bacteria) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Cystal structure of asparagine oxygenase in complex with Fe(II), 2S,3S-3-hydroxyasparagine and succinate
Overview
Non-ribosomally synthesized lipopeptide antibiotics of the daptomycin type are known to contain unnatural beta-modified amino acids, which are essential for bioactivity. Here we present the biochemical and structural basis for the incorporation of 3-hydroxyasparagine at position 9 in the 11-residue acidic lipopeptide lactone calcium-dependent antibiotic (CDA). Direct hydroxylation of l-asparagine by AsnO, a non-heme Fe(2+)/alpha-ketoglutarate-dependent oxygenase encoded by the CDA biosynthesis gene cluster, was validated by Fmoc derivatization of the reaction product and LC/MS analysis. The 1.45, 1.92, and 1.66 A crystal structures of AsnO as apoprotein, Fe(2+) complex, and product complex, respectively, with (2S,3S)-3-hydroxyasparagine and succinate revealed the stereoselectivity and substrate specificity of AsnO. The comparison of native and product-complex structures of AsnO showed a lid-like region (residues F208-E223) that seals the active site upon substrate binding and shields it from sterically demanding peptide substrates. Accordingly, beta-hydroxylated asparagine is synthesized prior to its incorporation into the growing CDA peptide. The AsnO structure could serve as a template for engineering novel enzymes for the synthesis of beta-hydroxylated amino acids.
About this Structure
2OG7 is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
Reference
Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide., Strieker M, Kopp F, Mahlert C, Essen LO, Marahiel MA, ACS Chem Biol. 2007 Mar 20;2(3):187-96. PMID:17373765
Page seeded by OCA on Thu Mar 20 17:59:17 2008
